Research workbench
Structure of lipoteichoic acid synthase ltas from listeria monocytogenes
Analyse Structure of lipoteichoic acid synthase ltas from listeria monocytogenes in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4UOO
- Type
- protein
- Length
- 2,075 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lipoteichoic acid synthase
- EC
- 2.7.8.-
- UniProt
- Q8Y8H6
- Ligands
- MG
- Pockets
- 20 · best druggability 0.67
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E | Lipoteichoic acid synthase (EC 2.7.8.-) | protein | 415 | 37% helix, 16% strand | Q8Y8H6 |
Ligands and binding sites
- MG · Magnesium ion · metal · 5 copies · chains A, B, C, D, E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 546 | 0.67 | 0.78 | 48 | empty |
| 2 | 672 | 0.63 | 0.73 | 68 | empty |
| 3 | 209 | 0.51 | 0.77 | 21 | empty |
| 4 | 207 | 0.50 | 0.76 | 23 | empty |
| 5 | 220 | 0.50 | 0.75 | 24 | empty |
Interfaces
5 interfaces between chains.
- A–E · 768 Ų buried · 11 hydrogen bonds · protein-protein
- B–E · 526 Ų buried · 10 hydrogen bonds · protein-protein
- C–D · 524 Ų buried · 12 hydrogen bonds · protein-protein
- D–E · 118 Ų buried · 3 hydrogen bonds · protein-protein
- C–E · 104 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 5 modified (phosphorylation).
Compared structures
- 4UOO · Structure of lipoteichoic acid synthase LtaS from Listeria monocytogenes · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q8Y8H6
- Elsewhere: RCSB PDB 4UOO · PDBe 4UOO · UniProt Q8Y8H6
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